issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

August 2020 issue

Highlighted illustration

Cover illustration: One of three structures of closely related NTF2-like superfamily proteins determined by Vuksanovic et al. [(2020), Acta Cryst. F76, 372-383]. The presence of a solvent-accessible cavity and the conservation of the His/Asp dyad suggest a potential enzymatic role for these enzymes in polyketide biosynthesis.

research communications


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FYCO1 plays an important role in the kinesin-dependent microtubule plus-end-directed transport of autophagosomes. Here, the crystal structure of the RUN domain of FYCO1 has been determined.

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The structure of the FAD-containing ferredoxin reductase FdR9 from Thermobifida fusca was obtained at 1.9 Å resolution.

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The crystal structure of GH30-7 endoxylanase C from the filamentous fungus Talaromyces cellulolyticus was determined at 1.65 Å resolution. Structural and mutational analyses revealed that subsite −2b possesses unique structural features that interact with arabinofuranosyl and 4-O-methyl-α-D-glucuronosyl side chains in a xylan substrate.

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The binding of CVT-313 to cyclin-dependent kinase 2 (CDK2) was confirmed using a thermal shift assay and its cellular potency was demonstrated in a CTG-based cell-proliferation assay. The crystal structure of the CDK2–CVT-313 complex was solved to a resolution of 1.74 Å. The structural information obtained from this study is expected to facilitate the design of more potent and selective CDK2 inhibitors for the treatment of cancer.

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The structure of the uncomplexed Rab-binding domain of Rab11 family-interacting protein 2 has been determined at 2.3 Å resolution. The structure reveals antiparallel α-helical dimers that associate in the crystal lattice through polar interactions. The dimers assemble into a four-helix bundle in the lattice that is brought together by a remarkable stack of arginine residues.

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The crystal structure of the aminoglycoside 6′-N-acetyltransferase from Enterococcus faecium is reported in a novel substrate-free form in order to understand the mechanism underlying its substrate recognition in detail. It is proposed that the enzyme sequentially undergoes conformational selection and induced fit for substrate binding.

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The structures of three closely related NTF2-like superfamily proteins that are involved in type II polyketide biosynthesis in as-yet-unknown ways were determined. The presence of a solvent-accessible cavity and the conservation of the His/Asp dyad suggest a potential enzymatic role for these enzymes in polyketide biosynthesis.

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The crystal structure of the extracellular domain of TMK3 shows that the non-leucine-rich-repeat region plays an essential role in its integrity.
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